期刊
CHEMISTRY & BIOLOGY
卷 22, 期 8, 页码 1008-1017出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2015.06.024
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资金
- Medical Research Council [MR/L000148/1]
- Engineering and Physical Sciences Research Council [EP/J021199/1] Funding Source: researchfish
- Medical Research Council [MR/L000148/1] Funding Source: researchfish
- EPSRC [EP/J021199/1] Funding Source: UKRI
- MRC [MR/L000148/1] Funding Source: UKRI
Protein fatty acylation regulates diverse aspects of cellular function and organization and plays a key role in host immune responses to infection. Acylation also modulates the function and localization of virus-encoded proteins. Here, we employ chemical proteomics tools, bio-orthogonal probes, and capture reagents to study myristoylation and palmitoylation during infection with herpes simplex virus (HSV). Using in-gel fluorescence imaging and quantitative mass spectrometry, we demonstrate a generalized reduction in myristoylation of host proteins, whereas palmitoylation of host proteins, including regulators of interferon and tetraspanin family proteins, was selectively repressed. Furthermore, we found that a significant fraction of the viral proteome undergoes palmitoylation; we identified a number of virus membrane glycoproteins, structural proteins, and kinases. Taken together, our results provide broad oversight of protein acylation during HSV infection, a roadmap for similar analysis in other systems, and a resource with which to pursue specific analysis of systems and functions.
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